With the recent completion of analysis of the human genome, much attention is now shifting to the field of proteomics, where gene products (proteins), their variants, interacting partners and the dynamics of their regulation and processing are the emphasis of study. Such studies are essential in understanding, for example, the mechanisms behind genetic/and environmentally induced disorders or the influences of drug mediated therapies, as well as potentially becoming the underlying foundation for further clinical and diagnostic analyses. Critical to these studies is the ability to qualitatively determine specific variants of whole proteins (e.g., splice variants, point mutations, post-translationally modified versions, and environmentally/therapeutically-induced modifications) and the ability to view their quantitative modulation. Moreover, it is becoming increasingly important to perform these analyses from not just one, but multiple biological fluids/extracts. There are limited methods of multiplexed protein measurement technologies due to the additional challenges inherent in protein samples.
However, measurement of proteins in biological fluid is difficult due to their inherent properties. Accordingly, there is a pressing need for rapid, sensitive, reproducible, and accurate analytical approaches for the analysis of proteins and their variants.
In order to analyze proteins of interest from—and in—their native environment, assays capable of assessing proteins present in a variety of biological fluids and/or extracts, both qualitatively and quantitatively, are needed.